Thesis (Ph. D.)--University of Missouri-Columbia, 2001. / Typescript. Vita. Includes bibliographical references. Also available on the Internet.

Diss. (sammanfattning) Stockholm : Karolinska institutet, 2009.

Thesis (Ph. D.)--University of Texas at Austin, 2006. / Vita. Includes bibliographical references.

Thesis (Ph. D.)--University of Missouri-Columbia, 1999. / Typescript. Vita. Includes bibliographical references (leaves 246-266). Also available on the Internet.

Xia Lixin. / "August 2004." / Thesis (Ph.D.)--Chinese University of Hong Kong, 2004. / Includes bibliographical references (p. 210-224). / Electronic reproduction. Hong Kong : Chinese University of Hong Kong, [2012] System requirements: Adobe Acrobat Reader. Available via World Wide Web. / Mode of access: World Wide Web. / Abstracts in English and Chinese.

by Mock Wai Yin. / Thesis (M.Phil.)--Chinese University of Hong Kong, 1996. / Includes bibliographical references (leaves 112-122). / ACKNOWLEDGEMENTS --- p.I / ABSTRACT --- p.II / TABLE OF CONTENT --- p.IV / Chapter CHAPTER 1: --- INTRODUCTION --- p.1 / Chapter CHAPTER 2: --- PURIFICATION OF α- AND β-MMCs --- p.29 / Chapter CHAPTER 3: --- RIBONUCLEASE ACTIVITY OF MMCs --- p.50 / Chapter CHAPTER 4: --- PURIFICATION AND RIBONUCLEASE ACTIVITY OF RNase-MC --- p.85 / Chapter CHAPTER 5: --- CONCLUSION --- p.109 / REFERENCES --- p.112

La primera part d'aquest treball s´ha centrat en la caracterització i optimització del procés d'activació de l´onconasa recombinant per tal d'obtenir l´enzim igual a la forma nativa. Per això, les reaccions d'eliminació de la Met-1 i la ciclació de la Glu1, necessàries per generar el piroglutamic han estat seguides per MALDI-TOF MS. La segona part d´aquest treball s´ha centrat en l´estudi de la contribució del pont disulfur 30-75 de l´onconasa a les seves propietats biològiques. Els resultats suggereixen que el potencial redox del citosol cel·lular podria reduir el pont disulfur 30-75 de l´onconasa salvatge afectant la unió onconasa -inhibidor proteic de ribonucleases. La tercera part ha consistit en la construcció de variants de l´HP-RNasa i onconasa amb activitat bactericida. Per això, s´ha introduït el determinant bactericida (YRWR) descrit per la proteïna catiònica d'eosinòfils en els dos enzims. Els resultats obtinguts han evidenciat que les dues ribonucleases amb el determinant bactericida presenten activitat citotòxica contra bacteris gram-negatius preferentment. / The first part of this work has been focused on the characterization and optimization of the activation process of the recombinant onconase to get an enzyme analogous to the native form. For this, Met-1 removal and Glu1 cyclization have been followed by MALDI-TOF MS. The second part of this work is focused on the study of the contribution of the 30-75 disulfide bond of onconase to its biological properties. The results suggest that the redox potential of the cytosol could reduce the disulfide bond 30-75 affecting the binding of onconase-ribonuclease inhibitor. The third part has been focused on the construction of HP-RNase and onconase variants endowed with bactericidal activity. For this, we have introduced a bactericidal (YRWR) determinant described for eosinophil cationic protein onto both enzymes. The resulting variants have bactericidal activity against gram-negative bacteria.

Diss. (sammanfattning) Stockholm : Karol. inst., 2004. / Härtill 5 uppsatser.

Not available / text

Ribonuclease II (RNase II) is a bacterial enzyme responsible for 90% of the exonucleolytic degradation of mRNA in bacteria, and has bacterial homologues known to be involved in virulence. The goal of this project was to examine the structural dynamics of RNase II using fluorescence. Prior to the beginning of this project, little was known regarding the structural composition of RNase II – required information in the study of structural dynamics. Consequently, the structure of RNase II was studied by constructing a series of deletion mutants in order to map the domains. The publication of an atomic resolution structure of RNase II allowed the project to move directly into the study of RNase II structural dynamics as it degrades mRNA. As a step towards this, RNase II was fluorescently labeled, and preliminary binding studies of DNA – a competitive inhibitor – to RNase II using fluorescence were conducted. / xii, 90 leaves : ill. (some col.) ; 29 cm